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Crystal structure of the glycopeptide N-methyltransferase mtfa

Analyse Crystal structure of the glycopeptide N-methyltransferase mtfa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G2M
Type: protein
Length: 446 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PCZA361.24
UniProt: O52805
Pockets: 6 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PCZA361.24	protein	232	31% helix, 33% strand	O52805
B	PCZA361.24	protein	214	32% helix, 36% strand	O52805

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	677	0.68	0.76	73	empty
2	182	0.53	0.79	31	empty
3	96	0.37	0.75	22	empty
4	84	0.35	0.75	20	empty
5	88	0.31	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 1557 Å² buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3G2M · Crystal Structure of the Glycopeptide N-methyltransferase MtfA · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O52805
Elsewhere: RCSB PDB 3G2M · PDBe 3G2M · UniProt O52805

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